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Ribose 1,5-bisphosphate isomerase (R15P isomerase) (R15Pi) (EC 5.3.1.29) (Ribulose 1,5-bisphosphate synthase) (RuBP synthase)

 R15PI_HALVD             Reviewed;         323 AA.
D4GV73;
10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 1.
22-NOV-2017, entry version 42.
RecName: Full=Ribose 1,5-bisphosphate isomerase;
Short=R15P isomerase;
Short=R15Pi;
EC=5.3.1.29;
AltName: Full=Ribulose 1,5-bisphosphate synthase;
Short=RuBP synthase;
OrderedLocusNames=HVO_0966;
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC
14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae;
Haloferax.
NCBI_TaxID=309800;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
VKM B-1768 / DS2;
PubMed=20333302; DOI=10.1371/journal.pone.0009605;
Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S.,
Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M.,
Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T.,
Eisen J.A.;
"The complete genome sequence of Haloferax volcanii DS2, a model
archaeon.";
PLoS ONE 5:E9605-E9605(2010).
[2]
SAMPYLATION AT LYS-210, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20054389; DOI=10.1038/nature08659;
Humbard M.A., Miranda H.V., Lim J.M., Krause D.J., Pritz J.R.,
Zhou G., Chen S., Wells L., Maupin-Furlow J.A.;
"Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax
volcanii.";
Nature 463:54-60(2010).
-!- FUNCTION: Catalyzes the isomerization of ribose 1,5-bisphosphate
(R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and
substrate for RubisCO. Functions in an archaeal AMP degradation
pathway, together with AMP phosphorylase and RubisCO (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Alpha-D-ribose 1,5-bisphosphate = D-ribulose
1,5-bisphosphate.
-!- MISCELLANEOUS: Reaction proceeds via a cis-phosphoenolate
intermediate. {ECO:0000250}.
-!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits
family. R15P isomerase subfamily. {ECO:0000305}.
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EMBL; CP001956; ADE03061.1; -; Genomic_DNA.
RefSeq; WP_004043979.1; NZ_AOHU01000094.1.
ProteinModelPortal; D4GV73; -.
SMR; D4GV73; -.
STRING; 309800.HVO_0966; -.
EnsemblBacteria; ADE03061; ADE03061; HVO_0966.
GeneID; 8925565; -.
KEGG; hvo:HVO_0966; -.
eggNOG; arCOG01124; Archaea.
eggNOG; COG1184; LUCA.
HOGENOM; HOG000224731; -.
KO; K18237; -.
OMA; DSAVRYF; -.
OrthoDB; POG093Z06II; -.
BioCyc; HVOL309800:GCOK-968-MONOMER; -.
Proteomes; UP000008243; Chromosome.
GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0044249; P:cellular biosynthetic process; IEA:InterPro.
Gene3D; 1.20.120.420; -; 1.
InterPro; IPR000649; IF-2B-related.
InterPro; IPR011559; Initiation_fac_2B_a/b/d.
InterPro; IPR027363; M1Pi_N.
InterPro; IPR037171; NagB/RpiA_transferase-like.
InterPro; IPR005250; Ribulose_e2b2.
Pfam; PF01008; IF-2B; 1.
SUPFAM; SSF100950; SSF100950; 1.
TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
TIGRFAMs; TIGR00511; ribulose_e2b2; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Complete proteome; Isomerase;
Isopeptide bond; Reference proteome; Ubl conjugation.
CHAIN 1 323 Ribose 1,5-bisphosphate isomerase.
/FTId=PRO_0000397103.
REGION 22 25 Substrate binding. {ECO:0000250}.
REGION 132 134 Substrate binding. {ECO:0000250}.
REGION 209 210 Substrate binding. {ECO:0000250}.
ACT_SITE 130 130 Proton acceptor. {ECO:0000250}.
ACT_SITE 199 199 Proton donor. {ECO:0000250}.
BINDING 65 65 Substrate. {ECO:0000250}.
BINDING 235 235 Substrate. {ECO:0000250}.
CROSSLNK 210 210 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SAMP2).
{ECO:0000269|PubMed:20054389}.
SEQUENCE 323 AA; 34876 MW; 27BA4853C01818A9 CRC64;
MDDRVHPEVR RTATEIDTME IRGAATIADA AARALRTQAT ESDAADAEAF RAELRATART
LHETRPTAVS LPNALRYVLR DMSSTTVEGL RQSVVDSADE FCARLERAQA DLGQVGANRL
RDGDTIMTHC HSTDALACVE AAVEQGKHIE AVVKETRPRN QGHITAKRLH ELGVPVTLIV
DSAARRYLND VDHVLVGADA VAADGSVINK IGTSGLAVNA RERGTPIMVA AQTLKLHPGT
MTGHTVDIEM RDTAEVVDDD TLADLGNPTV KNPAFDVTPP RYVDAIVTER GQFPPESIVI
LMRELFGEGT SEPWAEPSPR AEP


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